Sie befinden Sich nicht im Netzwerk der Universität Paderborn. Der Zugriff auf elektronische Ressourcen ist gegebenenfalls nur via VPN oder Shibboleth (DFN-AAI) möglich.
mehr Informationen...
Short α‐peptides with less than 10 residues generally display a low propensity to nucleate stable helical conformations. While various strategies to stabilize peptide helices have been previously reported, the ability of non‐peptide helical foldamers to stabilize α‐helices when fused to short α‐peptide segments has not been investigated. Towards this end, structural investigations into a series of chimeric oligomers obtained by joining aliphatic oligoureas to the C‐ or N‐termini of α‐peptides are described. All chimeras were found to be fully helical, with as few as 2 (or 3) urea units sufficient to propagate an α‐helical conformation in the fused peptide segment. The remarkable compatibility of α‐peptides with oligoureas described here, along with the simplicity of the approach, highlights the potential of interfacing natural and non‐peptide backbones as a means to further control the behavior of α‐peptides.
Konformative Symbiose: Nichtnatürliche heterogene Peptid‐Rückgrate, die durch Fusion von peptidmimetischen Harnstoff‐basierten helikalen Foldameren an eines der beiden Enden eines α‐Peptidsegments erhalten wurden, falten in eine helikale Struktur, welche die gesamte Sequenz unterbrechungsfrei umfasst. Schon wenige Harnstoffeinheiten genügen, um eine helikale Konformation entlang kurzer Peptidsegment fortzupflanzen.